Q59NB8 (LKHA4_CANAL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Leukotriene A-4 hydrolase homolog
Short name=LTA-4 hydrolase
EC=3.3.2.6

Alternative name(s):
Leukotriene A(4) hydrolase

Gene names

Name:	LKH1
ORF Names:	CaO19.992, CaO19.8607

Organism

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

Taxonomic identifier

237561 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length	623 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Aminopeptidase that preferentially cleaves tripeptides. Also has low epoxide hydrolase activity (in vitro). Can hydrolyze an epoxide moiety of LTA4 to form LTB4 (in vitro) By similarity.
Catalytic activity	(7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H2O = (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate.
Cofactor	Binds 1 zinc ion per subunit By similarity.
Pathway	Lipid metabolism; leukotriene B4 biosynthesis.
Subcellular location	Cytoplasm By similarity. Nucleus By similarity.
Sequence similarities	Belongs to the peptidase M1 family.

Ontologies

Keywords
Biological process	Leukotriene biosynthesis
Cellular component	Cytoplasm Nucleus
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
Gene Ontology (GO)
Biological process	leukotriene biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW peptide catabolic process Inferred from sequence or structural similarity. Source: UniProtKB proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	aminopeptidase activity Inferred from sequence or structural similarity. Source: UniProtKB epoxide hydrolase activity Inferred from sequence or structural similarity. Source: UniProtKB leukotriene-A4 hydrolase activity Inferred from electronic annotation. Source: EC metallopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 623	623	Leukotriene A-4 hydrolase homolog		PRO_0000324924
Regions
	Region	136 – 138	3	Substrate binding By similarity
	Region	261 – 266	6	Substrate binding By similarity
Sites
	Active site	291	1	Proton acceptor By similarity
	Active site	391	1	Proton donor By similarity
	Metal binding	290	1	Zinc; catalytic By similarity
	Metal binding	294	1	Zinc; catalytic By similarity
	Metal binding	313	1	Zinc; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q59NB8 [UniParc]. Last modified April 26, 2005. Version 1. Checksum: DAAAC0380CBA2D6C	FASTA	623	71,436
	10 20 30 40 50 60 MTRAIVESIK KRFHELDPCT NSNYSKFKVI HTDLTLTVSF ESKTLDGTVV YDLKNLDNAS 70 80 90 100 110 120 EVILDTSALN IKSTKVNGKE VSFELKPVTP IYGAPLRIPI NPNESEIQVE ISFTTTDKCT 130 140 150 160 170 180 AIQFIQGDTG PYVFSQCEAI HARSLFPCFD TPAVKSPYKF TGHSPAVVTM SGRAQPTDEP 190 200 210 220 230 240 NTYHFDQPIP IPSYLVSITS GNLLKAPIGP RSDVYSEEPS LKKCQWEFEK DMENFIQIAE 250 260 270 280 290 300 KIVFEYEWSR FDSLVLPSSF PYGGMEIPNM TQLTPTLISG DRTQTKVMAH ELAHSWSGNL 310 320 330 340 350 360 VTNSSWEHFW LNEGWTVYLE RRIIGAIAAA EAKEEGRKDA EKYGEQVRHF NMINGWNELA 370 380 390 400 410 420 DTCETFDKRY TKLVLDLENG DPDDSFSRIP YEKGFFFLYH LETKLGGIKE FDPFIKYYFN 430 440 450 460 470 480 KFKYQSLNTA QFVDTLYEFY EPKGKAEILD NIDWETWLFV SGLPEKPEFD VTLANQVYAL 490 500 510 520 530 540 VDKWVAYVKN GGELPGDETA DFEGEQDMLF LETLTEKFKT LDVKPEIIRL FPEIYPKYGA 550 560 570 580 590 600 SKNGEIISRW NELLISYGKY SSQDTLVQSF ASWLGTIGRM KYVRPGYLLL RKGISHEFAL 610 620 EVFKKYEHIY HPICRTMVKK DLS

References

[1]

"The diploid genome sequence of Candida albicans." Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S. Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed: 15123810] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SC5314 / ATCC MYA-2876.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AACQ01000208 Genomic DNA. Translation: EAK91971.1. AACQ01000207 Genomic DNA. Translation: EAK91995.1.
RefSeq	XP_711210.1. XM_706118.1. XP_711233.1. XM_706141.1.
3D structure databases
HSSP	HSSP built from PDB template 1HS6 based on UniProtKB P09960.
ProteinModelPortal	Q59NB8.
ModBase	Search...
Protein-protein interaction databases
STRING	Q59NB8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3647173. 3647187.
KEGG	cal:CaO19.8607. cal:CaO19.992.
Organism-specific databases
CGD	CAL0003842. LKH1.
Phylogenomic databases
PhylomeDB	Q59NB8.
Family and domain databases
InterPro	IPR016024. ARM-type_fold. IPR012777. Leukotriene_A4_hydrolase. IPR001930. Peptidase_M1. IPR015211. Peptidase_M1_C. IPR014782. Peptidase_M1_N. [Graphical view]
KO	K01254.
PANTHER	PTHR11533. Peptidase_M1. 1 hit.
Pfam	PF09127. Leuk-A4-hydro_C. 1 hit. PF01433. Peptidase_M1. 1 hit. [Graphical view]
PRINTS	PR00756. ALADIPTASE.
SUPFAM	SSF48371. ARM-type_fold. 1 hit.
TIGRFAMs	TIGR02411. Leuko_A4_hydro. 1 hit.
PROSITE	PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LKHA4_CANAL

Accession

Primary (citable) accession number: Q59NB8

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	April 26, 2005
Last modified:	January 25, 2012
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program